http://2008.igem.org/wiki/index.php?title=Team:Peking_University/Project&feed=atom&action=historyTeam:Peking University/Project - Revision history2024-03-28T22:10:59ZRevision history for this page on the wikiMediaWiki 1.16.5http://2008.igem.org/wiki/index.php?title=Team:Peking_University/Project&diff=105288&oldid=prevWendy at 05:26, 30 October 20082008-10-30T05:26:50Z<p></p>
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</table>Wendyhttp://2008.igem.org/wiki/index.php?title=Team:Peking_University/Project&diff=105105&oldid=prevWendy at 04:56, 30 October 20082008-10-30T04:56:20Z<p></p>
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</table>Wendyhttp://2008.igem.org/wiki/index.php?title=Team:Peking_University/Project&diff=105033&oldid=prevWendy at 04:49, 30 October 20082008-10-30T04:49:59Z<p></p>
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</table>Wendyhttp://2008.igem.org/wiki/index.php?title=Team:Peking_University/Project&diff=104990&oldid=prevLv.yuanye: /* Schematic Overview of Results */2008-10-30T04:46:32Z<p><span class="autocomment">Schematic Overview of Results</span></p>
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<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>''''' Jayanta Chaudhuri & Frederick W. Alt, Nature Reviews Immunology 4, 541-552 (July 2004)'''<br>''</div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>''''' Jayanta Chaudhuri & Frederick W. Alt, Nature Reviews Immunology 4, 541-552 (July 2004)'''<br>''</div></td></tr>
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<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div>[[Image:3 component-3 08.jpg|<del class="diffchange diffchange-inline">800px</del>]]<br></div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div>[[Image:3 component-3 08.jpg|<ins class="diffchange diffchange-inline">700px</ins>]]<br></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>'''In mammalian immune cells, hAID acts in cooperation with many trans-acting factors, likely to be DNA binding protein partners in the active SHM protein complex. Our approach harnesses an alternative strategy by fusion of DNA binding domain to directly target hAID onto a specific DNA loci. '''<br></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>'''In mammalian immune cells, hAID acts in cooperation with many trans-acting factors, likely to be DNA binding protein partners in the active SHM protein complex. Our approach harnesses an alternative strategy by fusion of DNA binding domain to directly target hAID onto a specific DNA loci. '''<br></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>'''''Valerie H. Odegard & David G. Schatz, Nature Reviews Immunology 6, 573-583 (August 2006)'''<br>''</div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>'''''Valerie H. Odegard & David G. Schatz, Nature Reviews Immunology 6, 573-583 (August 2006)'''<br>''</div></td></tr>
</table>Lv.yuanyehttp://2008.igem.org/wiki/index.php?title=Team:Peking_University/Project&diff=104841&oldid=prevWendy at 04:35, 30 October 20082008-10-30T04:35:56Z<p></p>
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</table>Wendyhttp://2008.igem.org/wiki/index.php?title=Team:Peking_University/Project&diff=104792&oldid=prevLv.yuanye: /* Schematic Overview of Results */2008-10-30T04:31:58Z<p><span class="autocomment">Schematic Overview of Results</span></p>
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<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>== Schematic Overview of Results ==</div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>== Schematic Overview of Results ==</div></td></tr>
<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div>[[Image:3 component-3 09.jpg|<del class="diffchange diffchange-inline">500px</del>]]<br></div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div>[[Image:3 component-3 09.jpg|<ins class="diffchange diffchange-inline">700px</ins>]]<br></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>'''Crystal structure of APO2 which is supposed to have similar structure of hAID.''' <br></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>'''Crystal structure of APO2 which is supposed to have similar structure of hAID.''' <br></div></td></tr>
<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div>[[Image:3 component-3 07.jpg|<del class="diffchange diffchange-inline">800px</del>]]<br></div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div>[[Image:3 component-3 07.jpg|<ins class="diffchange diffchange-inline">700px</ins>]]<br></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>'''Schematic structure of hAID, showing the N-terminal as catalytic active domain and C-terminal as protein-protein interaction domain. We choosed to fuse the DNA binding domain to hAID C-terminal based on this structure-activity relationship.''' <br></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>'''Schematic structure of hAID, showing the N-terminal as catalytic active domain and C-terminal as protein-protein interaction domain. We choosed to fuse the DNA binding domain to hAID C-terminal based on this structure-activity relationship.''' <br></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>''''' Jayanta Chaudhuri & Frederick W. Alt, Nature Reviews Immunology 4, 541-552 (July 2004)'''<br>''</div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>''''' Jayanta Chaudhuri & Frederick W. Alt, Nature Reviews Immunology 4, 541-552 (July 2004)'''<br>''</div></td></tr>
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<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>'''''Valerie H. Odegard & David G. Schatz, Nature Reviews Immunology 6, 573-583 (August 2006)'''<br>''</div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>'''''Valerie H. Odegard & David G. Schatz, Nature Reviews Immunology 6, 573-583 (August 2006)'''<br>''</div></td></tr>
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<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div>[[Image:3 component-3 01.jpg|<del class="diffchange diffchange-inline">800px</del>]]<br></div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div>[[Image:3 component-3 01.jpg|<ins class="diffchange diffchange-inline">500px</ins>]]<br></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>'''The dysfunctional Gal4(C77T) is under the control of pAct. The fusion protein hAID-lexA DBD specifically binds to the lexO region flanking the 3' of Gal4(C77T). With the facilitation of the linker, hAID is able to target to Gal4(C77T). '''<br></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>'''The dysfunctional Gal4(C77T) is under the control of pAct. The fusion protein hAID-lexA DBD specifically binds to the lexO region flanking the 3' of Gal4(C77T). With the facilitation of the linker, hAID is able to target to Gal4(C77T). '''<br></div></td></tr>
<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div>[[Image:3 component-3 02.jpg|<del class="diffchange diffchange-inline">800px</del>]]<br></div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div>[[Image:3 component-3 02.jpg|<ins class="diffchange diffchange-inline">500px</ins>]]<br></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>'''The Gal4(C77T) has lost the of DNA binding activity, so it failed to induce the expression of lacI; when Gal4(C77T) is mutated until it has restored its original function, it activates the expression of lacI. '''<br></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>'''The Gal4(C77T) has lost the of DNA binding activity, so it failed to induce the expression of lacI; when Gal4(C77T) is mutated until it has restored its original function, it activates the expression of lacI. '''<br></div></td></tr>
<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div>[[Image:3 component-3 03.jpg|<del class="diffchange diffchange-inline">800px</del>]]<br></div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div>[[Image:3 component-3 03.jpg|<ins class="diffchange diffchange-inline">500px</ins>]]<br></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>'''The expression of hAID is regulated by LacI. When lacI is expressed, expression of hAID is attenuated. ''' <br></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>'''The expression of hAID is regulated by LacI. When lacI is expressed, expression of hAID is attenuated. ''' <br></div></td></tr>
<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div>[[Image:3 component-3 04.jpg|<del class="diffchange diffchange-inline">800px</del>]]<br></div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div>[[Image:3 component-3 04.jpg|<ins class="diffchange diffchange-inline">500px</ins>]]<br></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>'''The triad relationship between the three components of our genetic circuit.'''<br> </div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>'''The triad relationship between the three components of our genetic circuit.'''<br> </div></td></tr>
<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div>[[Image:3 component-3 05.jpg|<del class="diffchange diffchange-inline">800px</del>]]<br></div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div>[[Image:3 component-3 05.jpg|<ins class="diffchange diffchange-inline">500px</ins>]]<br></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>'''For yeast screening process, two different reporters are used. His3 is used to report the viability of yeast strain. Functional Gal4 is able to induce the expression of His3 which enables the yeast strain to survive on the His- medium. Another reporter gene lacZ will enable us to use blue and white screening based on X-Gal plate.''' <br><br><br><br></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>'''For yeast screening process, two different reporters are used. His3 is used to report the viability of yeast strain. Functional Gal4 is able to induce the expression of His3 which enables the yeast strain to survive on the His- medium. Another reporter gene lacZ will enable us to use blue and white screening based on X-Gal plate.''' <br><br><br><br></div></td></tr>
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</table>Lv.yuanyehttp://2008.igem.org/wiki/index.php?title=Team:Peking_University/Project&diff=104706&oldid=prevWendy: /* Schematic Overview of Results */2008-10-30T04:24:44Z<p><span class="autocomment">Schematic Overview of Results</span></p>
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<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>== Schematic Overview of Results ==</div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>== Schematic Overview of Results ==</div></td></tr>
<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div>[[Image:3 component-3 09.jpg|<del class="diffchange diffchange-inline">800px</del>]]<br></div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div>[[Image:3 component-3 09.jpg|<ins class="diffchange diffchange-inline">500px</ins>]]<br></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>'''Crystal structure of APO2 which is supposed to have similar structure of hAID.''' <br></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>'''Crystal structure of APO2 which is supposed to have similar structure of hAID.''' <br></div></td></tr>
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</table>Wendyhttp://2008.igem.org/wiki/index.php?title=Team:Peking_University/Project&diff=104292&oldid=prevWendy at 04:01, 30 October 20082008-10-30T04:01:08Z<p></p>
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</table>Wendyhttp://2008.igem.org/wiki/index.php?title=Team:Peking_University/Project&diff=104089&oldid=prevHeculase: /* The Results */2008-10-30T03:55:54Z<p><span class="autocomment">The Results</span></p>
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<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div>'''Detailed view of P26 region of Gal4 in a Gal4-DNA complex structure. P26 is the outmost amino acid in the turning region of Gal4 helix DNA binding domain, and is essential for maintaining the structural motif needed to form coordination bond with Zn2+ ion (the yellow particle). Further more, the five-element ring structure of this proline has critical role to stablize the structure of Zinc finger domain. Replacing the proline to <del class="diffchange diffchange-inline">lysine </del>drastically alters the structure and nullifies DNA binding function of Gal4. This structure-based theoretical prediction is consistent with our experiment result -- yeast strains containing Gal4(C77T) but without hAID or its fusion protein failed to grow on histidine free medium. '''<br><br><br></div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div>'''Detailed view of P26 region of Gal4 in a Gal4-DNA complex structure. P26 is the outmost amino acid in the turning region of Gal4 helix DNA binding domain, and is essential for maintaining the structural motif needed to form coordination bond with Zn2+ ion (the yellow particle). Further more, the five-element ring structure of this proline has critical role to stablize the structure of Zinc finger domain. Replacing the proline to <ins class="diffchange diffchange-inline">leucine </ins>drastically alters the structure and nullifies DNA binding function of Gal4. This structure-based theoretical prediction is consistent with our experiment result -- yeast strains containing Gal4(C77T) but without hAID or its fusion protein failed to grow on histidine free medium. '''<br><br><br></div></td></tr>
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<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>All strains were inoculated into liquid medium in which the concentration of histidine gradually reduced during the week’s long screening. Then, cells were plated on agar plates containing NO His to test their viability ([[Media:Yeast Screening Model Plate.JPG|See figure]]). The culturing of the yeast and the plating used the following protocols. </div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>All strains were inoculated into liquid medium in which the concentration of histidine gradually reduced during the week’s long screening. Then, cells were plated on agar plates containing NO His to test their viability ([[Media:Yeast Screening Model Plate.JPG|See figure]]). The culturing of the yeast and the plating used the following protocols. </div></td></tr>
</table>Heculasehttp://2008.igem.org/wiki/index.php?title=Team:Peking_University/Project&diff=103981&oldid=prevWendy at 03:53, 30 October 20082008-10-30T03:53:19Z<p></p>
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</table>Wendy